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Volumn 80, Issue 17, 2006, Pages 8613-8626

Endoplasmic reticulum stress and neurodegeneration in rats neonatally infected with borna disease virus

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; COMPLEMENTARY DNA; INITIATION FACTOR 2ALPHA; MESSENGER RNA;

EID: 33748667752     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00836-06     Document Type: Article
Times cited : (68)

References (79)
  • 1
    • 23444443039 scopus 로고
    • CHOP (GADD153) and its oncogenic variant, TLS-CHOP, have opposing effects on the induction of G1/S arrest
    • Barone, M. V., A. Crozat, A. Tabaee, L. Philipson, and D. Ron. 1994. CHOP (GADD153) and its oncogenic variant, TLS-CHOP, have opposing effects on the induction of G1/S arrest. Genes Dev. 8:453-464.
    • (1994) Genes Dev. , vol.8 , pp. 453-464
    • Barone, M.V.1    Crozat, A.2    Tabaee, A.3    Philipson, L.4    Ron, D.5
  • 3
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Y. Zhang, L. M. Hendershot, H. P. Harding, and D. Ron. 2000. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2:326-332.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 4
    • 0034476896 scopus 로고    scopus 로고
    • An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus
    • Bitko, V., and S. Batik. 2001. An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus. J. Cell. Biochem. 80:441-454.
    • (2001) J. Cell. Biochem. , vol.80 , pp. 441-454
    • Bitko, V.1    Batik, S.2
  • 6
    • 0028821059 scopus 로고
    • Enzyme-linked immunosorbent assay for detecting antibodies to Borna disease virus-specific proteins
    • Briese, T., C. G. Hatalski, S. Kliche, Y. S. Park, and W. I. Lipkin. 1995. Enzyme-linked immunosorbent assay for detecting antibodies to Borna disease virus-specific proteins. J. Clin. Microbiol. 33:348-351.
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 348-351
    • Briese, T.1    Hatalski, C.G.2    Kliche, S.3    Park, Y.S.4    Lipkin, W.I.5
  • 7
    • 0024467317 scopus 로고
    • Astrocytes and Schwann cells are virus-host cells in the nervous system of rats with Borna disease
    • Carbone, K. M., B. D. Trapp, J. W. Griffin, C. S. Duchala, and O. Narayan. 1989. Astrocytes and Schwann cells are virus-host cells in the nervous system of rats with Borna disease. J. Neuropathol. Exp. Neurol. 48:631-644.
    • (1989) J. Neuropathol. Exp. Neurol. , vol.48 , pp. 631-644
    • Carbone, K.M.1    Trapp, B.D.2    Griffin, J.W.3    Duchala, C.S.4    Narayan, O.5
  • 9
    • 19944432792 scopus 로고    scopus 로고
    • Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+ ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells
    • Cardozo, A. K., F. Ortis, J. Storling, Y. M. Feng, J. Rasschaert, M. Tonnesen, F. Van Eylen, T. Mandrup-Poulsen, A. Herchuelz, and D. L. Eizirik. 2005. Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+ ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells. Diabetes 54:452-461.
    • (2005) Diabetes , vol.54 , pp. 452-461
    • Cardozo, A.K.1    Ortis, F.2    Storling, J.3    Feng, Y.M.4    Rasschaert, J.5    Tonnesen, M.6    Van Eylen, F.7    Mandrup-Poulsen, T.8    Herchuelz, A.9    Eizirik, D.L.10
  • 11
    • 0027937969 scopus 로고
    • Molecular biology of borna disease virus: Prototype of a new group of animal viruses
    • de la Torre, J. C. 1994. Molecular biology of borna disease virus: prototype of a new group of animal viruses. J. Virol. 68:7669-7675.
    • (1994) J. Virol. , vol.68 , pp. 7669-7675
    • De La Torre, J.C.1
  • 12
    • 0242492706 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration
    • Dimcheff, D. E., S. Askovic, A. H. Baker, C. Johnson-Fowler, and J. L. Portis. 2003. Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration. J. Virol. 77:12617-12629.
    • (2003) J. Virol. , vol.77 , pp. 12617-12629
    • Dimcheff, D.E.1    Askovic, S.2    Baker, A.H.3    Johnson-Fowler, C.4    Portis, J.L.5
  • 13
    • 4043077042 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) stress induced by a neurovirulent mouse retrovirus is associated with prolonged BiP binding and retention of a viral protein in the ER
    • Dimcheff, D. E., M. A. Faasse, F. J. McAtee, and J. L. Portis. 2004. Endoplasmic reticulum (ER) stress induced by a neurovirulent mouse retrovirus is associated with prolonged BiP binding and retention of a viral protein in the ER. J. Biol. Chem. 279:33782-33790.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33782-33790
    • Dimcheff, D.E.1    Faasse, M.A.2    McAtee, F.J.3    Portis, J.L.4
  • 15
    • 0042707870 scopus 로고    scopus 로고
    • Dysregulated ryanodine receptors mediate cellular toxicity: Restoration of normal phenotype by FKBP12.6
    • George, C. H., G. V. Higgs, J. J. Mackrill, and F. A. Lai. 2003. Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6. J. Biol. Chem. 278:28856-28864.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28856-28864
    • George, C.H.1    Higgs, G.V.2    Mackrill, J.J.3    Lai, F.A.4
  • 16
    • 23644436847 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control and apoptosis
    • Groenendyk, J., and M. Michalak. 2005. Endoplasmic reticulum quality control and apoptosis. Acta Biochim. Pol. 52:381-395.
    • (2005) Acta Biochim. Pol. , vol.52 , pp. 381-395
    • Groenendyk, J.1    Michalak, M.2
  • 17
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • Harding, H. P., Y. Zhang, and D. Ron. 1999. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397:271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 18
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H. P., I. Novoa, Y. Zhang, H. Zeng, R. Wek, M. Schapira, and D. Ron. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6:1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 20
    • 0032191623 scopus 로고    scopus 로고
    • Evolution of the immune response in the central nervous system following infection with Borna disease virus
    • Hatalski, C. G., W. F. Hickey, and W. I. Lipkin. 1998. Evolution of the immune response in the central nervous system following infection with Borna disease virus. J. Neuroimmunol. 90:137-142.
    • (1998) J. Neuroimmunol. , vol.90 , pp. 137-142
    • Hatalski, C.G.1    Hickey, W.F.2    Lipkin, W.I.3
  • 21
    • 11844282198 scopus 로고    scopus 로고
    • Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons
    • Hayashi, T., A. Saito, S. Okuno, M. Ferrand-Drake, R. L. Dodd, and P. H. Chan. 2005. Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons. J. Cereb. Blood Flow Metab. 25:41-53.
    • (2005) J. Cereb. Blood Flow Metab. , vol.25 , pp. 41-53
    • Hayashi, T.1    Saito, A.2    Okuno, S.3    Ferrand-Drake, M.4    Dodd, R.L.5    Chan, P.H.6
  • 22
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze, K., H. Yoshida, H. Yanagi, T. Yura, and K. Mon. 1999. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell. 10:3787-3799.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mon, K.5
  • 23
    • 0031017382 scopus 로고    scopus 로고
    • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • He, B., M. Gross, and B. Roizman. 1997. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl. Acad. Sci. USA 94:843-848.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 24
    • 13244300647 scopus 로고    scopus 로고
    • Exposure of astrocytes to hypoxia/reoxygenation enhances expression of glucose-regulated protein 78 facilitating astrocyte release of the neuroprotective cytokine interleukin 6
    • Hori, O., M. Matsumoto, K. Kuwabara, Y. Maeda, H. Ueda, T. Ohtsuki, T. Kinoshita, S. Ogawa, D. M. Stern, and T. Kamada. 1996. Exposure of astrocytes to hypoxia/reoxygenation enhances expression of glucose-regulated protein 78 facilitating astrocyte release of the neuroprotective cytokine interleukin 6. J. Neurochem. 66:973-979.
    • (1996) J. Neurochem. , vol.66 , pp. 973-979
    • Hori, O.1    Matsumoto, M.2    Kuwabara, K.3    Maeda, Y.4    Ueda, H.5    Ohtsuki, T.6    Kinoshita, T.7    Ogawa, S.8    Stern, D.M.9    Kamada, T.10
  • 26
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler, J. A., A. H. Skalet, and J. C. Alwine. 2005. Human cytomegalovirus infection activates and regulates the unfolded protein response. J. Virol. 79:6890-6899.
    • (2005) J. Virol. , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 27
    • 0036776317 scopus 로고    scopus 로고
    • Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells
    • Jordan, R., L. Wang, T. M. Graczyk, T. M. Block, and P. R. Romano. 2002. Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells. J. Virol. 76:9588-9599.
    • (2002) J. Virol. , vol.76 , pp. 9588-9599
    • Jordan, R.1    Wang, L.2    Graczyk, T.M.3    Block, T.M.4    Romano, P.R.5
  • 28
    • 0037199911 scopus 로고    scopus 로고
    • Tumor necrosis factor induces apoptosis in hepatoma cells by increasing Ca(2+) release from the endoplasmic reticulum and suppressing Bcl-2 expression
    • Kim, B. C., H. T. Kim, M. Mamura, I. S. Ambudkar, K. S. Choi, and S. J. Kim. 2002. Tumor necrosis factor induces apoptosis in hepatoma cells by increasing Ca(2+) release from the endoplasmic reticulum and suppressing Bcl-2 expression. J. Biol. Chem. 277:31381-31389.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31381-31389
    • Kim, B.C.1    Kim, H.T.2    Mamura, M.3    Ambudkar, I.S.4    Choi, K.S.5    Kim, S.J.6
  • 29
    • 3042638296 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulum stress signaling pathway is associated with neuronal degeneration in MoMuLV-ts1-induced spongiform encephalomyelopathy
    • Kim, H. T., K. Waters, G. Stoica, W. Qiang, N. Liu, V. L. Scofield, and P. K. Wong. 2004. Activation of endoplasmic reticulum stress signaling pathway is associated with neuronal degeneration in MoMuLV-ts1-induced spongiform encephalomyelopathy. Lab. Investig. 84:816-827.
    • (2004) Lab. Investig. , vol.84 , pp. 816-827
    • Kim, H.T.1    Waters, K.2    Stoica, G.3    Qiang, W.4    Liu, N.5    Scofield, V.L.6    Wong, P.K.7
  • 32
    • 33745677648 scopus 로고    scopus 로고
    • Comparative study of endoplasmic reticulum stress-induced neuronal death in rat cultured hippocampal and cerebellar granule neurons
    • Epub ahead of print
    • Kosuge, Y., T. Sakikubo, K. Ishige, and Y. Ito. 2006. Comparative study of endoplasmic reticulum stress-induced neuronal death in rat cultured hippocampal and cerebellar granule neurons. Neurochem. Int. [Epub ahead of print.]
    • (2006) Neurochem. Int.
    • Kosuge, Y.1    Sakikubo, T.2    Ishige, K.3    Ito, Y.4
  • 33
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., M. Segal, K. Normington, M. J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332:462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 34
    • 33244496230 scopus 로고    scopus 로고
    • Emergence of endoplasmic reticulum stress and activated microglia in Purkinje cell degeneration mice
    • Kyuhou, S. I., N. Kato, and H. Gemba. 2006. Emergence of endoplasmic reticulum stress and activated microglia in Purkinje cell degeneration mice. Neurosci. Lett. 396:91-96.
    • (2006) Neurosci. Lett. , vol.396 , pp. 91-96
    • Kyuhou, S.I.1    Kato, N.2    Gemba, H.3
  • 35
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A. H., N. N. Iwakoshi, and L. H. Glimcher. 2003. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23:7448-7459.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 36
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee, A. S. 2005. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 35:373-381.
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 37
    • 20444390622 scopus 로고    scopus 로고
    • The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers
    • Li, F., T. Hayashi, G. Jin, K. Deguchi, S. Nagotani, I. Nagano, M. Shoji, P. H. Chan, and K. Abe. 2005. The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers. Brain Res. 1048:59-68.
    • (2005) Brain Res. , vol.1048 , pp. 59-68
    • Li, F.1    Hayashi, T.2    Jin, G.3    Deguchi, K.4    Nagotani, S.5    Nagano, I.6    Shoji, M.7    Chan, P.H.8    Abe, K.9
  • 38
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: Thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • Li, M., P. Baumeister, B. Roy, T. Phan, D. Foti, S. Luo, and A. S. Lee. 2000. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol. Cell. Biol. 20:5096-5106.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6    Lee, A.S.7
  • 39
    • 13544263363 scopus 로고    scopus 로고
    • Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells
    • Li, X. D., H. Lankinen, N. Putkuri, O. Vapalahti, and A. Vaheri. 2005. Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells. Virology 333:180-189.
    • (2005) Virology , vol.333 , pp. 180-189
    • Li, X.D.1    Lankinen, H.2    Putkuri, N.3    Vapalahti, O.4    Vaheri, A.5
  • 40
    • 0032947436 scopus 로고    scopus 로고
    • Activation of the grp78 and grp94 promoters by hepatitis C virus E2 envelope protein
    • Liberman, E., Y. L. Fong, M. J. Selby, Q. L. Choo, L. Cousens, M. Houghton, and T. S. Yen. 1999. Activation of the grp78 and grp94 promoters by hepatitis C virus E2 envelope protein. J. Virol. 73:3718-3722.
    • (1999) J. Virol. , vol.73 , pp. 3718-3722
    • Liberman, E.1    Fong, Y.L.2    Selby, M.J.3    Choo, Q.L.4    Cousens, L.5    Houghton, M.6    Yen, T.S.7
  • 41
  • 42
    • 0141621215 scopus 로고    scopus 로고
    • Induction of Grp78/BiP by translational block: Activation of the Grp78 promoter by ATF4 through an upstream ATF/CRE site independent of the endoplasmic reticulum stress elements
    • Luo, S., P. Baumeister, S. Yang, S. F. Abcouwer, and A. S. Lee. 2003. Induction of Grp78/BiP by translational block: activation of the Grp78 promoter by ATF4 through an upstream ATF/CRE site independent of the endoplasmic reticulum stress elements. J. Biol. Chem. 278:37375-37385.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37375-37385
    • Luo, S.1    Baumeister, P.2    Yang, S.3    Abcouwer, S.F.4    Lee, A.S.5
  • 43
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles, M. M., and H. F. Gilbert. 1991. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30:613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 44
    • 0030597160 scopus 로고    scopus 로고
    • Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells
    • Matsumoto, M., M. Minami, K. Takeda, Y. Sakao, and S. Akira. 1996. Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells. FEBS Lett. 395:143-147.
    • (1996) FEBS Lett. , vol.395 , pp. 143-147
    • Matsumoto, M.1    Minami, M.2    Takeda, K.3    Sakao, Y.4    Akira, S.5
  • 45
    • 0035879276 scopus 로고    scopus 로고
    • Stress-inducible transcription factor CHOP/gadd153 induces apoptosis in mammalian cells via p38 kinase-dependent and -independent mechanisms
    • Maytin, E. V., M. Ubeda, J. C. Lin, and J. F. Habener. 2001. Stress-inducible transcription factor CHOP/gadd153 induces apoptosis in mammalian cells via p38 kinase-dependent and -independent mechanisms. Exp. Cell. Res. 267:193-204.
    • (2001) Exp. Cell. Res. , vol.267 , pp. 193-204
    • Maytin, E.V.1    Ubeda, M.2    Lin, J.C.3    Habener, J.F.4
  • 46
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough, K. D., J. L. Martindale, L. O. Klotz, T. Y. Aw, and N. J. Holbrook. 2001. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 21:1249-1259.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 47
    • 0020616022 scopus 로고
    • Behavioral disease in rats caused by immunopathological responses to persistent borna virus in the brain
    • Narayan, O., S. Herzog, K. Frese, H. Scheefers, and R. Rott. 1983. Behavioral disease in rats caused by immunopathological responses to persistent borna virus in the brain. Science 220:1401-1403.
    • (1983) Science , vol.220 , pp. 1401-1403
    • Narayan, O.1    Herzog, S.2    Frese, K.3    Scheefers, H.4    Rott, R.5
  • 48
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada, T., H. Yoshida, R. Akazawa, M. Negishi, and K. Mori. 2002. Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 366:585-594.
    • (2002) Biochem. J. , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 49
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari, S., and M. Mori. 2004. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 11:381-389.
    • (2004) Cell Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 50
    • 0034733043 scopus 로고    scopus 로고
    • Depletion of intracellular Ca2+ by caffeine and ryanodine induces apoptosis of Chinese hamster ovary cells transfected with ryanodine receptor
    • Pan, Z., D. Damron, A. L. Nieminen, M. B. Bhat, and J. Ma. 2000. Depletion of intracellular Ca2+ by caffeine and ryanodine induces apoptosis of Chinese hamster ovary cells transfected with ryanodine receptor. J. Biol. Chem. 275:19978-19984.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19978-19984
    • Pan, Z.1    Damron, D.2    Nieminen, A.L.3    Bhat, M.B.4    Ma, J.5
  • 51
    • 0037320172 scopus 로고    scopus 로고
    • Loading neurons with BAPTA-AM activates xbp1 processing indicative of induction of endoplasmic reticulum stress
    • Paschen, W., S. Hotop, and C. Aufenberg. 2003. Loading neurons with BAPTA-AM activates xbp1 processing indicative of induction of endoplasmic reticulum stress. Cell Calcium 33:83-89.
    • (2003) Cell Calcium , vol.33 , pp. 83-89
    • Paschen, W.1    Hotop, S.2    Aufenberg, C.3
  • 52
    • 0037333913 scopus 로고    scopus 로고
    • Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2α kinase PERK
    • Pavio, N., P. R. Romano, T. M. Graczyk, S. M. Feinstone, and D. R. Taylor. 2003. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2α kinase PERK. J. Virol. 77:3578-3585.
    • (2003) J. Virol. , vol.77 , pp. 3578-3585
    • Pavio, N.1    Romano, P.R.2    Graczyk, T.M.3    Feinstone, S.M.4    Taylor, D.R.5
  • 53
    • 0033180091 scopus 로고    scopus 로고
    • Persistent Borna disease virus infection of neonatal rats causes brain regional changes of mRNAs for cytokines, cytokine receptor components and neuropeptides
    • Plata-Salaman, C. R., S. E. Ilyin, D. Gayle, A. Romanovitch, and K. M. Carbone. 1999. Persistent Borna disease virus infection of neonatal rats causes brain regional changes of mRNAs for cytokines, cytokine receptor components and neuropeptides. Brain Res. Bull. 49:441-451.
    • (1999) Brain Res. Bull. , vol.49 , pp. 441-451
    • Plata-Salaman, C.R.1    Ilyin, S.E.2    Gayle, D.3    Romanovitch, A.4    Carbone, K.M.5
  • 54
    • 0033954390 scopus 로고    scopus 로고
    • Effects of neonatal rat Borna disease virus (BDV) infection on the postnatal development of the brain monoaminergic systems
    • Pletnikov, M. V., S. A. Rubin, G. J. Schwartz, K. M. Carbone, and T. H. Moran. 2000. Effects of neonatal rat Borna disease virus (BDV) infection on the postnatal development of the brain monoaminergic systems. Brain Res. Dev. Brain Res. 119:179-185.
    • (2000) Brain Res. Dev. Brain Res. , vol.119 , pp. 179-185
    • Pletnikov, M.V.1    Rubin, S.A.2    Schwartz, G.J.3    Carbone, K.M.4    Moran, T.H.5
  • 55
    • 33645235475 scopus 로고    scopus 로고
    • Astrocytes survive chronic infection and cytopathic effects of the ts1 mutant of the retrovirus Moloney murine leukemia virus by upregulation of antioxidant defenses
    • Qiang, W., X. Kuang, J. Liu, N. Liu, V. L. Scofield, A. J. Reid, Y. Jiang, G. Stoica, W. S. Lynn, and P. K. Wong. 2006. Astrocytes survive chronic infection and cytopathic effects of the ts1 mutant of the retrovirus Moloney murine leukemia virus by upregulation of antioxidant defenses. J. Virol. 80:3273-3284.
    • (2006) J. Virol. , vol.80 , pp. 3273-3284
    • Qiang, W.1    Kuang, X.2    Liu, J.3    Liu, N.4    Scofield, V.L.5    Reid, A.J.6    Jiang, Y.7    Stoica, G.8    Lynn, W.S.9    Wong, P.K.10
  • 56
    • 0042477717 scopus 로고    scopus 로고
    • Gene expression during ER stress-induced apoptosis in neurons: Induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway
    • Reimertz, C., D. Kogel, A. Rami, T. Chittenden, and J. H. Prehn. 2003. Gene expression during ER stress-induced apoptosis in neurons: induction of the BH3-only protein Bbc3/PUMA and activation of the mitochondrial apoptosis pathway. J. Cell Biol. 162:587-597.
    • (2003) J. Cell Biol. , vol.162 , pp. 587-597
    • Reimertz, C.1    Kogel, D.2    Rami, A.3    Chittenden, T.4    Prehn, J.H.5
  • 57
    • 2642647847 scopus 로고    scopus 로고
    • Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin
    • Richt, J. A., T. Furbringer, A. Koch, I. Pfeuffer, C. Herden, I. Bause-Niedrig, and W. Garten. 1998. Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin. J. Virol. 72:4528-4533.
    • (1998) J. Virol. , vol.72 , pp. 4528-4533
    • Richt, J.A.1    Furbringer, T.2    Koch, A.3    Pfeuffer, I.4    Herden, C.5    Bause-Niedrig, I.6    Garten, W.7
  • 58
    • 18944395787 scopus 로고    scopus 로고
    • Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT
    • Ritter, C., K. Quirin, M. Kowarik, and A. Helenius. 2005. Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT. EMBO J. 24:1730-1738.
    • (2005) EMBO J. , vol.24 , pp. 1730-1738
    • Ritter, C.1    Quirin, K.2    Kowarik, M.3    Helenius, A.4
  • 59
    • 0033119798 scopus 로고    scopus 로고
    • Cytokine expression in the rat central nervous system following perinatal Borna disease virus infection
    • Sauder, C., and J. C. de la Torre. 1999. Cytokine expression in the rat central nervous system following perinatal Borna disease virus infection. J. Neuroimmunol. 96:29-45.
    • (1999) J. Neuroimmunol. , vol.96 , pp. 29-45
    • Sauder, C.1    De La Torre, J.C.2
  • 61
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response
    • Schroder, M., and R. J. Kaufman. 2005. ER stress and the unfolded protein response. Mutat. Res. 569:29-63.
    • (2005) Mutat. Res. , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 62
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J., X. Chen, L. Hendershot, and R. Prywes. 2002. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3:99-111.
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 63
    • 0036223410 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response
    • Su, H. L., C. L. Liao, and Y. L. Lin. 2002. Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J. Virol. 76:4162-4171.
    • (2002) J. Virol. , vol.76 , pp. 4162-4171
    • Su, H.L.1    Liao, C.L.2    Lin, Y.L.3
  • 64
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • Tanaka, S., T. Uehara, and Y. Nomura. 2000. Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death. J. Biol. Chem. 275:10388-10393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 65
    • 0036314483 scopus 로고    scopus 로고
    • Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway
    • Tardif, K. D., K. Mori, and A. Siddiqui. 2002. Hepatitis C virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway. J. Virol. 76:7453-7459.
    • (2002) J. Virol. , vol.76 , pp. 7453-7459
    • Tardif, K.D.1    Mori, K.2    Siddiqui, A.3
  • 66
    • 2342435179 scopus 로고    scopus 로고
    • Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response
    • Tardif, K. D., K. Mori, R. J. Kaufman, and A. Siddiqui. 2004. Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J. Biol. Chem. 279:17158-17164.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17158-17164
    • Tardif, K.D.1    Mori, K.2    Kaufman, R.J.3    Siddiqui, A.4
  • 67
    • 0037036412 scopus 로고    scopus 로고
    • Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16
    • Thuerauf, D. J., L. E. Morrison, H. Hoover, and C. C. Glembotski. 2002. Coordination of ATF6-mediated transcription and ATF6 degradation by a domain that is shared with the viral transcription factor, VP16. J. Biol. Chem. 277:20734-20739.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20734-20739
    • Thuerauf, D.J.1    Morrison, L.E.2    Hoover, H.3    Glembotski, C.C.4
  • 68
    • 13944250933 scopus 로고    scopus 로고
    • Human cytomegalovirus protein US11 provokes an unfolded protein response that may facilitate the degradation of class I major histocompatibility complex products
    • Tirosh, B., N. N. Iwakoshi, B. N. Lilley, A. H. Lee, L. H. Glimcher, and H. L. Ploegh. 2005. Human cytomegalovirus protein US11 provokes an unfolded protein response that may facilitate the degradation of class I major histocompatibility complex products. J. Virol. 79:2768-2779.
    • (2005) J. Virol. , vol.79 , pp. 2768-2779
    • Tirosh, B.1    Iwakoshi, N.N.2    Lilley, B.N.3    Lee, A.H.4    Glimcher, L.H.5    Ploegh, H.L.6
  • 69
    • 26044431774 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium signaling in nerve cells
    • Verkhratsky, A. 2004. Endoplasmic reticulum calcium signaling in nerve cells. Biol. Res. 37:693-699.
    • (2004) Biol. Res. , vol.37 , pp. 693-699
    • Verkhratsky, A.1
  • 70
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase
    • Wang, X. Z., and D. Ron. 1996. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science 272:1347-1349.
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 72
    • 0034126901 scopus 로고    scopus 로고
    • Microglial activation and neuronal apoptosis in Bornavirus infected neonatal Lewis rats
    • Weissenbock, H., M. Hornig, W. F. Hickey, and W. I. Lipkin. 2000. Microglial activation and neuronal apoptosis in Bornavirus infected neonatal Lewis rats. Brain Pathol. 10:260-272.
    • (2000) Brain Pathol. , vol.10 , pp. 260-272
    • Weissenbock, H.1    Hornig, M.2    Hickey, W.F.3    Lipkin, W.I.4
  • 73
    • 0036366704 scopus 로고    scopus 로고
    • Why do Purkinje cells die so easily after global brain ischemia? Aldolase C, EAAT4, and the cerebellar contribution to posthypoxic myoclonus
    • Welsh, J. P., G. Yuen, D. G. Placantonakis, Y. Q. Vu, F. Haiss, E. O'Hearn, M. E. Molliver, and S. A. Aicher. 2002. Why do Purkinje cells die so easily after global brain ischemia? Aldolase C, EAAT4, and the cerebellar contribution to posthypoxic myoclonus. Adv. Neurol. 89:331-359.
    • (2002) Adv. Neurol. , vol.89 , pp. 331-359
    • Welsh, J.P.1    Yuen, G.2    Placantonakis, D.G.3    Vu, Y.Q.4    Haiss, F.5    O'Hearn, E.6    Molliver, M.E.7    Aicher, S.A.8
  • 74
    • 33646588302 scopus 로고    scopus 로고
    • Metallothioneins and zinc dysregulation contribute to neurodevelopmental damage in a model of perinatal viral infection
    • Williams, B. L., K. Yaddanapudi, C. M. Kirk, A. Soman, M. Hornig, and W. I. Lipkin. 2006. Metallothioneins and zinc dysregulation contribute to neurodevelopmental damage in a model of perinatal viral infection. Brain Pathol. 16:1-14.
    • (2006) Brain Pathol. , vol.16 , pp. 1-14
    • Williams, B.L.1    Yaddanapudi, K.2    Kirk, C.M.3    Soman, A.4    Hornig, M.5    Lipkin, W.I.6
  • 75
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye, J., R. B. Rawson, R. Komuro, X. Chen, U. P. Dave, R. Prywes, M. S. Brown, and J. L. Goldstein. 2000. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6:1355-1364.
    • (2000) Mol. Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6    Brown, M.S.7    Goldstein, J.L.8
  • 76
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida, H., K. Haze, H. Yanagi, T. Yura, and K. Mori. 1998. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273: 33741-33749.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 77
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida, H., T. Okada, K. Haze, H. Yanagi, T. Yura, M. Negishi, and K. Mori. 2000. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20:6755-6767.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7
  • 78
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H., T. Matsui, A. Yamamoto, T. Okada, and K. Mori. 2001. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 79
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao, L., C. Longo-Guess, B. S. Harris, J. W. Lee, and S. L. Ackerman. 2005. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37:974-979.
    • (2005) Nat. Genet. , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5


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